ID   T2BLB_BACSQ             Reviewed;         301 AA.
AC   Q9LAI0;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-MAY-2023, entry version 48.
DE   RecName: Full=Type II restriction enzyme BslI subunit beta {ECO:0000303|PubMed:12654995};
DE            Short=R.BslIbeta;
DE            EC=3.1.21.4 {ECO:0000269|PubMed:10648519};
DE   AltName: Full=Endonuclease BslI subunit beta;
DE   AltName: Full=Type IIT restriction enzyme BslI subunit beta;
DE   AltName: Full=Type-2 restriction enzyme BslI subunit beta;
GN   Name=bslIRbeta {ECO:0000303|PubMed:10648519};
OS   Bacillus sp. (strain NEB-606).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=114630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS,
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=10648519; DOI=10.1128/jb.182.4.949-955.2000;
RA   Hsieh P.-C., Xiao J.-P., O'Loane D., Xu S.-Y.;
RT   "Cloning, expression, and purification of a thermostable nonhomodimeric
RT   restriction enzyme, BslI.";
RL   J. Bacteriol. 182:949-955(2000).
RN   [2]
RP   ZINC-BINDING, ABSORPTION SPECTROSCOPY, AND MUTAGENESIS OF CYS-62; HIS-66;
RP   CYS-79 AND CYS-82.
RC   STRAIN=NEB-606;
RX   PubMed=14623197; DOI=10.1016/j.jmb.2003.09.043;
RA   Scheuring Vanamee E., Hsieh P.-C., Zhu Z., Yates D., Garman E., Xu S.-Y.,
RA   Aggarwal A.K.;
RT   "Glucocorticoid receptor-like Zn(Cys)4 motifs in BslI restriction
RT   endonuclease.";
RL   J. Mol. Biol. 334:595-603(2003).
RN   [3]
RP   NOMENCLATURE, AND SUBTYPE.
RX   PubMed=12654995; DOI=10.1093/nar/gkg274;
RA   Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A.,
RA   Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K.,
RA   Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S.,
RA   Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A.,
RA   Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S.,
RA   Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V.,
RA   Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E.,
RA   Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W.,
RA   Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.;
RT   "A nomenclature for restriction enzymes, DNA methyltransferases, homing
RT   endonucleases and their genes.";
RL   Nucleic Acids Res. 31:1805-1812(2003).
CC   -!- FUNCTION: A P subtype restriction enzyme that recognizes the double-
CC       stranded sequence 5'-CCN(7)GG-3' and cleaves after N-7.
CC       {ECO:0000269|PubMed:10648519, ECO:0000303|PubMed:12654995}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage of DNA to give specific double-
CC         stranded fragments with terminal 5'-phosphates.; EC=3.1.21.4;
CC         Evidence={ECO:0000269|PubMed:10648519};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:14623197};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Is one of the thermostable restriction enzymes that remain active
CC         after 20 to 30 cycles of thermal PCR cycling.;
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits. The alpha
CC       subunit is believed to be responsible for DNA recognition, while the
CC       beta subunit is thought to mediate cleavage.
CC       {ECO:0000269|PubMed:10648519}.
CC   -!- BIOTECHNOLOGY: Could be used to screen carcinogenic mutations in a
CC       restriction endonuclease-mediated selective PCR (or REMS-PCR) assay. In
CC       particular, could be used to detect the vast majority of mutations that
CC       occur at codons 12 or 13 of the Ras oncogenes that encode glycine
CC       (codons GGN) at those positions.
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DR   EMBL; AF135191; AAF32531.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9LAI0; -.
DR   REBASE; 386; BslI.
DR   PRO; PR:Q9LAI0; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009036; F:type II site-specific deoxyribonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Endonuclease; Hydrolase; Metal-binding;
KW   Nuclease; Restriction system; Zinc; Zinc-finger.
FT   CHAIN           1..301
FT                   /note="Type II restriction enzyme BslI subunit beta"
FT                   /id="PRO_0000077284"
FT   ZN_FING         62..82
FT                   /note="CHC2-type"
FT   MUTAGEN         62
FT                   /note="C->K: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:14623197"
FT   MUTAGEN         66
FT                   /note="H->K: 50% of wild-type activity."
FT                   /evidence="ECO:0000269|PubMed:14623197"
FT   MUTAGEN         79
FT                   /note="C->K: 10% of wild-type activity."
FT                   /evidence="ECO:0000269|PubMed:14623197"
FT   MUTAGEN         82
FT                   /note="C->K: 10% of wild-type activity."
FT                   /evidence="ECO:0000269|PubMed:14623197"
SQ   SEQUENCE   301 AA;  35272 MW;  9EFAD4778F5E5A4C CRC64;
     MEQQKFPNPR IFEDIDATDF SKHNKKHVTE DFVAENFKDV GWRVYRPFND TGIDLIAKKF
     VCPDGHTKWN QNLTKEMTCS ECGKSLIEIT RFIQVKTREV KQVKTREAKG EKFFFGYTLK
     SKDFRTDPRH VFLLYSDFTM DFIILPMYDY LNLFYTNQSL GSTHFSTPSF RQGNNKLNGL
     SKDKNDNWVW SGVSFNEFVN EKGMDKLSCP IYDIELESYT KKIQELKFSL FYRYSPGRKN
     QVSAPTVEFI NNHFSIFISL PKEAIASKRK AHLESLRQDL PEDLKKSVNE GYLVKFKGVD
     L
//